UBE2H_MOUSE
ID UBE2H_MOUSE Reviewed; 183 AA.
AC P62257; P37286;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 H;
DE EC=2.3.2.23 {ECO:0000250|UniProtKB:P62256};
DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme H;
DE EC=2.3.2.24 {ECO:0000250|UniProtKB:P62256};
DE AltName: Full=E2 ubiquitin-conjugating enzyme H;
DE AltName: Full=UBCH2;
DE AltName: Full=Ubiquitin carrier protein H;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-20K {ECO:0000303|PubMed:7761435};
DE AltName: Full=Ubiquitin-protein ligase H;
GN Name=Ube2h;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=7761435; DOI=10.1073/pnas.92.11.4982;
RA Wefes I., Mastrandrea L.D., Haldeman M., Koury S.T., Tamburlin J.,
RA Pickart C.M., Finley D.;
RT "Induction of ubiquitin-conjugating enzymes during terminal erythroid
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4982-4986(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=7590289; DOI=10.1016/0378-1119(95)00374-f;
RA Wefes I., Kaiser P., Schneider R., Pickart C.M., Finley D.;
RT "Characterization of a cDNA clone encoding E2-20K, a murine ubiquitin-
RT conjugating enzyme.";
RL Gene 163:321-322(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. E2 ubiquitin conjugating enzyme
CC that transfers ubiquitin to MAEA, a core component of the CTLH E3
CC ubiquitin-protein ligase complex. In vitro catalyzes 'Lys-11'- and
CC 'Lys-48'-linked polyubiquitination. Capable, in vitro, to ubiquitinate
CC histone H2A. {ECO:0000250|UniProtKB:P62256}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000250|UniProtKB:P62256, ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:P62256};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with MAEA and WDR26, components of the CTLH complex
CC that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or
CC alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5.
CC {ECO:0000250|UniProtKB:P62256}.
CC -!- TISSUE SPECIFICITY: Detected in reticulocytes, lung, brain and skeletal
CC muscle (at protein level) (PubMed:7761435). Ubiquitous. Detected in
CC cardiac muscle, brain, spleen, lung, liver, skeletal muscle, kidney
CC andmso testis (PubMed:7590289). {ECO:0000269|PubMed:7590289,
CC ECO:0000269|PubMed:7761435}.
CC -!- PTM: Autoubiquitinated in vitro in the presence of NEDD4L.
CC {ECO:0000250|UniProtKB:P62256}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; U19854; AAA91975.1; -; mRNA.
DR EMBL; BC008517; AAH08517.1; -; mRNA.
DR CCDS; CCDS19969.1; -.
DR PIR; JC4308; JC4308.
DR RefSeq; NP_033485.1; NM_009459.3.
DR AlphaFoldDB; P62257; -.
DR SMR; P62257; -.
DR BioGRID; 204417; 9.
DR STRING; 10090.ENSMUSP00000100058; -.
DR iPTMnet; P62257; -.
DR PhosphoSitePlus; P62257; -.
DR EPD; P62257; -.
DR PaxDb; P62257; -.
DR PeptideAtlas; P62257; -.
DR PRIDE; P62257; -.
DR ProteomicsDB; 298181; -.
DR Antibodypedia; 1149; 210 antibodies from 29 providers.
DR DNASU; 22214; -.
DR Ensembl; ENSMUST00000102993; ENSMUSP00000100058; ENSMUSG00000039159.
DR GeneID; 22214; -.
DR KEGG; mmu:22214; -.
DR UCSC; uc009bey.3; mouse.
DR CTD; 7328; -.
DR MGI; MGI:104632; Ube2h.
DR VEuPathDB; HostDB:ENSMUSG00000039159; -.
DR eggNOG; KOG0416; Eukaryota.
DR GeneTree; ENSGT00390000004852; -.
DR HOGENOM; CLU_030988_7_5_1; -.
DR InParanoid; P62257; -.
DR OMA; EFCVKFY; -.
DR OrthoDB; 1301162at2759; -.
DR PhylomeDB; P62257; -.
DR TreeFam; TF101121; -.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22214; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Ube2h; mouse.
DR PRO; PR:P62257; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P62257; protein.
DR Bgee; ENSMUSG00000039159; Expressed in blood and 248 other tissues.
DR ExpressionAtlas; P62257; baseline and differential.
DR Genevisible; P62257; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IGI:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:MGI.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..183
FT /note="Ubiquitin-conjugating enzyme E2 H"
FT /id="PRO_0000082487"
FT DOMAIN 1..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 152..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 183 AA; 20655 MW; 3DD5D365945F708C CRC64;
MSSPSPGKRR MDTDVVKLIE SKHEVTILGG LNEFVVKFYG PQGTPYEGGV WKVRVDLPDK
YPFKSPSIGF MNKIFHPNID EASGTVCLDV INQTWTALYD LTNIFESFLP QLLAYPNPID
PLNGDAAAMY LHRPEEYKQK IKEYIQKYAT EEALKEQEEG TGDSSSESSM SDFSEDEAQD
MEL
